Solution structures of the double PHD fingers of human transcriptional protein DPF3 bound to a histone peptide containing acetylation at lysine 14. Determined by solution NMR. Released 14 Jul 2010.
Explore 2KWJ in 3D Show helices and sheets RCSB PDB PDBe
2KWJ contains 3 α-helices and 7 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 268 | 1 | 2 |
| β-strand | 271 | 1 | 2 |
| β-strand | 282-283 | 2 | 3 |
| β-strand | 290-291 | 2 | 3 |
| α-helix | 300-308 | 9 | |
| α-helix | 314-316 | 3 | |
| β-strand | 331-333 | 3 | 1 |
| β-strand | 340-342 | 3 | 1 |
| α-helix | 361-369 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone peptide | B | protein | 20 | P68431 (AlphaFold model) | |
| Zinc finger protein DPF3 | A | protein | 114 | Homo sapiens | Q92784 (AlphaFold model) |
>2KWJ_1 Histone peptide (chains B) ARTKQTARKSTGGKAPRKQL
>2KWJ_2 Zinc finger protein DPF3 (chains A) GSYCDFCLGGSNMNKKSGRPEELVSCADCGRSGHPTCLQFTLNMTEAVKTYKWQCIECKS CILCGTSENDDQLLFCDDCDRGYHMYCLNPPVAEPPEGSWSCHLCWELLKEKAS
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b. Zeng, L., Zhang, Q., Li, S. et al. Nature (2010) 466:258-262. DOI 10.1038/nature09139 · PubMed
Other PDB entries of the same protein (UniProt P68431 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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